RUMI_CULQU
ID RUMI_CULQU Reviewed; 403 AA.
AC B0X1Q4;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=O-glucosyltransferase rumi homolog;
DE EC=2.4.1.- {ECO:0000250|UniProtKB:Q8T045};
DE Flags: Precursor;
GN ORFNames=CPIJ013394;
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000312|EMBL:EDS38782.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000312|EMBL:EDS38782.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D.,
RA Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C.M., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protein O-glucosyltransferase. Catalyzes the reaction that
CC attaches glucose through an O-glycosidic linkage to a conserved serine
CC residue found in the consensus sequence C-X-S-X-[PA]-C in epidermal
CC growth factor-like repeats. Regulates Notch signaling by glucosylating
CC Notch in the ER, glucosylation is required for the correct folding and
CC cleavage of Notch. {ECO:0000250|UniProtKB:Q8T045}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q8T045}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:Q8T045}. Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 90 family.
CC {ECO:0000305}.
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DR EMBL; DS232266; EDS38782.1; -; Genomic_DNA.
DR RefSeq; XP_001863576.1; XM_001863541.1.
DR AlphaFoldDB; B0X1Q4; -.
DR SMR; B0X1Q4; -.
DR STRING; 7176.CPIJ013394-PA; -.
DR CAZy; GT90; Glycosyltransferase Family 90.
DR GeneID; 6046359; -.
DR KEGG; cqu:CpipJ_CPIJ013394; -.
DR VEuPathDB; VectorBase:CPIJ013394; -.
DR VEuPathDB; VectorBase:CQUJHB000226; -.
DR eggNOG; KOG2458; Eukaryota.
DR HOGENOM; CLU_041919_1_0_1; -.
DR InParanoid; B0X1Q4; -.
DR OMA; DHCQYKY; -.
DR OrthoDB; 1106728at2759; -.
DR PhylomeDB; B0X1Q4; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002320; Partially assembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0018242; P:protein O-linked glycosylation via serine; ISS:UniProtKB.
DR InterPro; IPR006598; CAP10.
DR Pfam; PF05686; Glyco_transf_90; 1.
DR SMART; SM00672; CAP10; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW Reference proteome; Secreted; Signal; Transferase.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..403
FT /note="O-glucosyltransferase rumi homolog"
FT /id="PRO_0000342691"
FT REGION 190..195
FT /note="Interaction with the consensus sequence C-X-S-X-
FT [PA]-C in peptide substrates"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT ACT_SITE 148
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT BINDING 227..231
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT BINDING 235
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT BINDING 274..276
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT BINDING 292..296
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT SITE 119
FT /note="Interaction with the consensus sequence C-X-S-X-
FT [PA]-C in peptide substrates"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT SITE 230
FT /note="Interaction with the consensus sequence C-X-S-X-
FT [PA]-C in peptide substrates"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT SITE 257
FT /note="Interaction with the consensus sequence C-X-S-X-
FT [PA]-C in peptide substrates"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 66..73
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT DISULFID 71..376
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT DISULFID 117..123
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT DISULFID 280..303
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
SQ SEQUENCE 403 AA; 47710 MW; 1C347622A983A8AF CRC64;
MQCIYFTSVL LVIFAQNGQT DDGGMCMAKE TCTETQQEAP TNNLYKAADN KYITLIEEAL
AAYKPCESSN CSCHLDVLKT DLRPFRSGIT QDLIELARSY GTKYQIIGHR MFRQRDCMFP
ARCSGVEHFI RPNLPKLPDM ELIINCRDWP QISRHWNASR EPLPVLSFSK TNDYLDIMYP
TWGFWEGGPA ISLYPTGLGR WDQHRVSVRK AAKVWPWEKK LQQAFFRGSR TSDERDPLVL
LSRMRPELVD AQYTKNQAWR SPKDTLHAEP AQEVRLEDHC QYKYLFNFRG VAASFRFKHL
FLCKSLVFHV GQEWQEFFYD SLKPWVHYVP VPVGINEWEL EHLIQFFREH DQLAQEIANR
GYEHIWNHLR MEDVECYWKR LLRRYGKLVK YEVKRDEELV EIF
